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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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関連する実験動画

Updated: Jun 22, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

マルチサイトリン酸化システムにおける無制限のマルチスタビリティ

Matthew Thomson1, Jeremy Gunawardena

  • 1Biophysics Program, Harvard University, Cambridge, Massachusetts 02138, USA.

Nature
|June 19, 2009
PubMed
まとめ
この要約は機械生成です。

マルチサイトタンパク質のリン酸化は,重要な規制メカニズムであり,複雑な信号ネットワークを生成することができます. この研究は,対立する酵素が,タンパク質のフォスフォ形式の明確な,安定した分布を生み出し,柔軟な細胞情報処理を可能にすることを明らかにしています.

さらに関連する動画

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

関連する実験動画

Last Updated: Jun 22, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

科学分野:

  • バイオケミストリーと分子生物学
  • システム生物学 システム生物学
  • 翻訳後の修正 翻訳後の修正

背景:

  • タンパク質の可逆性リン酸化は重要な翻訳後の改変であり,エウカリオットはプロカリオットよりもタンパク質あたりのリン酸化部位を大幅に多く示しています.
  • マルチサイトリン酸化により,指数関数的に多くのタンパク質のフォスフォ形式が生成され,それぞれが潜在的に異なる生物学的役割を持つ.
  • 細胞内のこれらの多様なフォスフォ形態の調節と分布は,ほとんど不明のままである.

研究 の 目的:

  • 異なったキナーゼとフォスファタゼの活動下で,マルチサイト基板のフォスフォ形態の安定状態分布を調査する.
  • 複雑なフォスフォプロテオームの規制の可能性と情報処理能力を探求する.
  • マルチサイトリン酸化ダイナミクスを分析するための簡素化された数学的枠組みを開発する.

主な方法:

  • マルチサイト基板におけるキナーゼとフォスファターゼの相反する活動の数学モデリング.
  • 安定状態のフォスフォフォーム濃度の幾何学的性質の分析.
  • 複雑な微分方程式シミュレーションの代わりに代数式方程式を導出する.

主要な成果:

  • マルチサイト基板に対する相反する酵素作用は,安定した状態で明確な安定したフォスフォ形式の分布につながる可能性があります.
  • 安定分布の数は,リン酸化部位の数 (n) により増加する.
  • フォスフォ形式の分布は焦点化または拡散可能であり,情報をエンコードできる流体調節ネットワークを示唆する.

結論:

  • リン型分布の可塑性は,真核細胞における複雑な情報処理のメカニズムを提供する.
  • 大量のリン酸化部位は,規制の可能性を増やすことにより,機能上の利点を与える可能性があります.
  • 新しい数学的アプローチにより,複合的な翻訳後の改変ネットワークに適用可能なマルチサイトリン酸化の分析が簡素化されています.